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Information on EC 1.14.13.24 - 3-hydroxybenzoate 6-monooxygenase and Organism(s) Pseudomonas alcaligenes and UniProt Accession Q9F131

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IUBMB Comments
A flavoprotein (FAD). Acts also on a number of analogues of 3-hydroxybenzoate substituted in the 2, 4, 5 and 6 positions; NADPH can act instead of NADH, but more slowly.
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This record set is specific for:
Pseudomonas alcaligenes
UNIPROT: Q9F131
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The taxonomic range for the selected organisms is: Pseudomonas alcaligenes
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
3-hydroxybenzoate 6-hydroxylase, 3hb6h, 3-hydroxybenzoate-6-hydroxylase, 3-hba-6-hydroxylase, ncgl2923, mnx2p, 3-hydroxybenzoate 6-monooxygenase, m-hydroxybenzoate 6-hydroxylase, 3-hydroxybenzoic acid-6-hydroxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-hydroxybenzoate-6-hydroxylase
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3-HBA-6-hydroxylase
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-
-
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3-hydroxybenzoate 6-hydroxylase
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-
-
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3-hydroxybenzoic acid-6-hydroxylase
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-
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m-hydroxybenzoate 6-hydroxylase
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oxygenase, 3-hydroxybenzoate 6-mono-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
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oxidation
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-
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reduction
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SYSTEMATIC NAME
IUBMB Comments
3-hydroxybenzoate,NADH:oxygen oxidoreductase (6-hydroxylating)
A flavoprotein (FAD). Acts also on a number of analogues of 3-hydroxybenzoate substituted in the 2, 4, 5 and 6 positions; NADPH can act instead of NADH, but more slowly.
CAS REGISTRY NUMBER
COMMENTARY hide
51570-26-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-aminobenzoate + NAD(P)H + O2
?
show the reaction diagram
-
-
-
?
3-bromobenzoate + NAD(P)H + O2
?
show the reaction diagram
-
-
-
?
3-chlorobenzoate + NAD(P)H + O2
?
show the reaction diagram
-
-
-
?
3-fluorobenzoate + NAD(P)H + O2
?
show the reaction diagram
-
-
-
?
3-hydroxy-3-methylbenzoate + NAD(P)H + O2
2,5-dihydroxy-3-methylbenzoate + NAD(P)+ + H2O
show the reaction diagram
-
-
-
?
3-hydroxy-4-methylbenzoate + NAD(P)H + O2
2,5-dihydroxy-4-methylbenzoate + NAD(P)+ + H2O
show the reaction diagram
the substrate is an intermediate in the degradation of 2,5-xylenol, higher activity with the recombinant His-tagged enzyme compared to the native enzyme
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-
?
3-hydroxy-5-methylbenzoate + NAD(P)H + O2
2,5-dihydroxy-3-methylbenzoate + NAD(P)+ + H2O
show the reaction diagram
the substrate is an intermediate in the degradation of 3,5-xylenol, higher activity with the recombinant His-tagged enzyme compared to the native enzyme, preferred substrate
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-
?
3-hydroxybenzoate + NAD(P)H + O2
2,5-dihydroxybenzoate + NAD(P)+ + H2O
show the reaction diagram
3-methylthiobenzoate + NAD(P)H + O2
?
show the reaction diagram
-
-
-
?
additional information
?
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degradation of 2,5-xylenol and 3,5-xylenol in strain P25X depends on isozyme I, not isozyme II
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-hydroxybenzoate + NAD(P)H + O2
2,5-dihydroxybenzoate + NAD(P)+ + H2O
show the reaction diagram
the enzyme is involved in the degradation of 2,5-xylenol and 3,5-xylenol via the gentisate pathway, overview
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-
?
additional information
?
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degradation of 2,5-xylenol and 3,5-xylenol in strain P25X depends on isozyme I, not isozyme II
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
XlnD can utilize either NADH or NADPH as the electron donor, NADH is preferred
NADPH
XlnD can utilize either NADH or NADPH as the electron donor, NADH is preferred
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
slight activation of 13% at 5 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
complete inhibition at 0.05 mM
Fe2+
complete inhibition at 5 mM
Hg2+
complete inhibition at 0.05 mM
Mn2+
complete inhibition at 5 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
isozyme II is strictly inducible by specific aromatic substrates
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.071 - 0.095
3-hydroxy-4-methylbenzoate
0.079 - 0.108
3-hydroxybenzoate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.63
recombinant His-tagged enzyme, substrate 3-hydroxy-5-methylbenzoate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 50
no activity below 15°C and above 50°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene xlnD, two isozymes I and II
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
effects of carbon sources for growth on enzyme substrate specificity, overview
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
3HBH1_PSEAC
394
1
43435
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
130000
His-tagged recombinant enzyme, native PAGE and gel filtration
43000
3 * 43000, His-tagged recombinant enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
3 * 43000, His-tagged recombinant enzyme, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
construction of a P25X xlnD knockout mutant strain G50, no induction after growth on lactate and 3-hydroxy-4-methylbenzoate in contrast to the wild-type enzyme, slightly reduced activity with 3-hydroxybenzoate and gentisate
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, purified recombinant enzyme, 50 mM MOPS or 100 mM potassium phosphate, 10% v/v glycerol, 0.2 mM FAD, 60% activity remaining after 3 months
22°C, rom temperature, purified recombinant enzyme, 50 mM MOPS or 100 mM potassium phosphate, 10% v/v glycerol, 0.2 mM FAD, complete loss of activity after 12 h
4°C, purified recombinant enzyme, 50 mM MOPS or 100 mM potassium phosphate, 10% v/v glycerol, 0.2 mM FAD, complete loss of activity after 3 days
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinnat His-tagged enzyme from Escherichia coli by metal chelating chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene xlnD, DNA and amino acid sequence determination and analysis, subcloning and overexpression of the His-tagged enzyme in Escherichia coli strain DH5alpha, S17-1, and BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gao, X.; Tan, C.L.; Yeo, C.C.; Poh, C.L.
Molecular and biochemical characterization of the xlnD-encoded 3-hydroxybenzoate 6-hydroxylase involved in the degradation of 2,5-xylenol via the gentisate pathway in Pseudomonas alcaligenes NCIMB 9867
J. Bacteriol.
187
7696-7702
2005
Pseudomonas alcaligenes (Q9F131), Pseudomonas alcaligenes P25X (Q9F131)
Manually annotated by BRENDA team